Product Name: BFAR Antibody
Species Reactivity: Human, Mouse, Rat
Tested Applications: ELISA, IF, IHC-P, WB
Applications: BFAR antibody can be used for detection of BFAR by Western blot at 1 – 2 μg/mL. Antibody can also be used for immunohistochemistry starting at 5 μg/mL. For immunofluorescence start at 20 μg/mL.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight:
Immunogen: BFAR antibody was raised against a 14 amino acid synthetic peptide near the carboxy terminus of human BFAR.The immunogen is located within amino acids 300 – 350 of BFAR.
Host Species: Rabbit
Purification: BFAR Antibody is affinity chromatography purified via peptide column.
Physical State: Liquid
CAS NO.: 6199-67-3
Product: Cucurbitacin B
Buffer: BFAR Antibody is supplied in PBS containing 0.02% sodium azide.
Concentration: 1 mg/mL
Storage Conditions: BFAR antibody can be stored at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: BFAR Antibody: BAR, RNF47, BAR, Bifunctional apoptosis regulator, RING finger protein 47
Accession NO.: NP_057645
Protein Ino: 7706091
Official Symbol: BFAR
Geneid: 51283
Background: BFAR Antibody: The bifunctional apoptosis inhibitor (BFAR) is scaffold protein that integrates signaling components of the cells apoptosis-regulatory machinery. BFAR is a multidomain protein capable of inhibiting apoptosis induced by TNF-family death receptors (extrinsic pathway) as well as mitochondria-dependent apoptosis (intrinsic pathway). Interaction of BFAR with Bcl-2 or Bcl-XL via a SAM domain may contribute to the anti-apoptotic properties of BFAR. In addition, BFAR contains a DED-like domain that is capable of suppressing apoptosis mediated at the receptor level. BFAR is also thought to be involved in the regulation of neuronal survival.
PubMed ID:http://aac.asm.org/content/42/2/447.abstract
